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Not to be confused with Hamilton Anxiety Rating Scale.
Protein HARS PDB 1x59.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases HARS, HRS, USH3B, CMT2W, histidyl-tRNA synthetase
External IDs MGI: 108087 HomoloGene: 1592 GeneCards: HARS
RNA expression pattern
PBB GE HARS 202042 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 5: 140.67 – 140.69 Mb Chr 18: 36.77 – 36.78 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene.[3][4]


Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins.[5] The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter.[3]

Clinical significance[edit]

The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.[5]


HARS has been shown to interact with EEF1B2[6] and EEF1G.[6]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: HARS histidyl-tRNA synthetase". 
  4. ^ Wasmuth JJ, Carlock LR (1986). "Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5". Somat. Cell Mol. Genet. 12 (5): 513–7. doi:10.1007/BF01539922. PMID 3464104. 
  5. ^ a b Freist W, Verhey JF, Rühlmann A, Gauss DH, Arnez JG (1999). "Histidyl-tRNA synthetase". Biol. Chem. 380 (6): 623–46. doi:10.1515/BC.1999.079. PMID 10430027. 
  6. ^ a b Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477. 

Further reading[edit]